ID   DJB12_BOVIN             Reviewed;         370 AA.
AC   Q58DR2;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=DnaJ homolog subfamily B member 12;
GN   Name=DNAJB12;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
CC   -!- FUNCTION: Acts as a co-chaperone with HSPA8/Hsc70; required to promote
CC       protein folding and trafficking, prevent aggregation of client
CC       proteins, and promote unfolded proteins to endoplasmic reticulum-
CC       associated degradation (ERAD) pathway. Acts by determining
CC       HSPA8/Hsc70's ATPase and polypeptide-binding activities. Can also act
CC       independently of HSPA8/Hsc70: together with DNAJB14, acts as a
CC       chaperone that promotes maturation of potassium channels KCND2 and
CC       KCNH2 by stabilizing nascent channel subunits and assembling them into
CC       tetramers. While stabilization of nascent channel proteins is dependent
CC       on HSPA8/Hsc70, the process of oligomerization of channel subunits is
CC       independent of HSPA8/Hsc70. When overexpressed, forms membranous
CC       structures together with DNAJB14 and HSPA8/Hsc70 within the nucleus;
CC       the role of these structures, named DJANGOs, is still unclear.
CC       {ECO:0000250|UniProtKB:Q9NXW2}.
CC   -!- SUBUNIT: Homodimer and homotetramer. Interacts (via J domain) with
CC       HSPA8/Hsc70. Forms a multiprotein complex, at least composed of
CC       DNAJB12, DNAJB14, HSPA8/Hsc70 and SGTA; interaction with DNAJB14 and
CC       HSPA8/Hsc70 is direct. {ECO:0000250|UniProtKB:Q9NXW2}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q9NXW2}; Single-pass membrane protein
CC       {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:Q9NXW2}; Single-
CC       pass membrane protein {ECO:0000250|UniProtKB:Q9NXW2}. Note=Localizes to
CC       the endoplasmic reticulum membrane. When overexpressed, forms
CC       membranous structures in the nucleus. {ECO:0000250|UniProtKB:Q9NXW2}.
CC   -!- PTM: Methylated at His-185 by METTL9. {ECO:0000250|UniProtKB:Q9NXW2}.
CC   -!- SIMILARITY: Belongs to the DnaJ family. DNAJB12/DNAJB14 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BT021535; AAX46382.1; -; mRNA.
DR   RefSeq; NP_001017946.1; NM_001017946.1.
DR   AlphaFoldDB; Q58DR2; -.
DR   SMR; Q58DR2; -.
DR   STRING; 9913.ENSBTAP00000018144; -.
DR   PaxDb; Q58DR2; -.
DR   PRIDE; Q58DR2; -.
DR   GeneID; 533603; -.
DR   KEGG; bta:533603; -.
DR   CTD; 54788; -.
DR   eggNOG; KOG0714; Eukaryota.
DR   InParanoid; Q58DR2; -.
DR   OrthoDB; 1173544at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030544; F:Hsp70 protein binding; IBA:GO_Central.
DR   GO; GO:0071218; P:cellular response to misfolded protein; ISS:UniProtKB.
DR   GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; ISS:UniProtKB.
DR   GO; GO:0036503; P:ERAD pathway; ISS:UniProtKB.
DR   GO; GO:0065003; P:protein-containing complex assembly; ISS:UniProtKB.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR   CDD; cd06257; DnaJ; 1.
DR   Gene3D; 1.10.287.110; -; 1.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR018253; DnaJ_domain_CS.
DR   InterPro; IPR015399; DUF1977_DnaJ-like.
DR   InterPro; IPR036869; J_dom_sf.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF09320; DUF1977; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; SSF46565; 1.
DR   PROSITE; PS00636; DNAJ_1; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Chaperone; Endoplasmic reticulum; Membrane; Methylation;
KW   Nucleus; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..370
FT                   /note="DnaJ homolog subfamily B member 12"
FT                   /id="PRO_0000253762"
FT   TRANSMEM        242..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          110..174
FT                   /note="J"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT   REGION          51..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..88
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NXW2"
FT   MOD_RES         185
FT                   /note="Pros-methylhistidine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NXW2"
SQ   SEQUENCE   370 AA;  41340 MW;  248F80639BA67EAB CRC64;
     MESNKDEAER CISIALKAIQ SNQPDRALRF LEKAQRLYPT PRVHALIESL NQKPQPAGDQ
     PQPTEATHTT HRKAAGANTA SANGEAGGES TKGYTAEQVA AVKRVKQCKD YYEILGVSRG
     ASDEDLKKAY RKLALKFHPD KNHAPGATEA FKAIGTAYAV LSNPEKRKQY DQFGDDKGQA
     ARHGHGHGDF HRGFEADISP EDLFNMFFGG GFPSSNVHVY SNGRMRYTYH QRQDRRENQG
     DGGLGVFVQL MPILILILVS ALSQLMVSSP PYSLSLRPSV GHVHKRVTDH LNVVYYVADT
     FSQEYTGSSL KMVERNVEDD YIANLRNNCW KEKQQKEGLL YRARYFGDAD MYNKAQKDGA
     PQAVTDCQRL